title: Biochemical differences between products of the Adh locus in Drosophila.
abstract: An analysis of the molecular properties of the major alcohol dehydrogenase (E.C.1.1.1.1.) allozyme variants found segregating in natural populations of D. melanogaster is presented. Our results indicate: (1) ADH-S enzyme has generally lower Michaelis-Menten constants than those of ADH-F; (2) ADH-S and ADH-F enzymes display opposite interactions for both co-factor and substrate; and (3) higher levels of ADH are associated with the Adh-fast genotype. The possible adaptive significance of these findings is discussed.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D004331:Drosophila melanogaster / Q000235:genetics*; D014644:Genetic Variation; D007700:Kinetics; D010641:Phenotype
chemical_list: D000429:Alcohol Oxidoreductases